Structure of a polyisoprenoid binding domain from Saccharophagus degradans implicated in plant cell wall breakdown

FEBS Lett. 2010 Apr 16;584(8):1577-84. doi: 10.1016/j.febslet.2010.03.015. Epub 2010 Mar 16.

Abstract

Saccharophagus degradans belongs to a recently discovered group of marine bacteria equipped with an arsenal of sugar cleaving enzymes coupled to carbohydrate-binding domains to degrade various insoluble complex polysaccharides. The modular Sde-1182 protein consists of a family 2 carbohydrate binding module linked to a X158 domain of unknown function. The 1.9 A and 1.55 A resolution crystal structures of the isolated X158 domain bound to the two related polyisoprenoid molecules, ubiquinone and octaprenyl pyrophosphate, unveil a beta-barrel architecture reminiscent of the YceI-like superfamily that resembles the architecture of the lipocalin fold. This unprecedented association coupling oxidoreduction and carbohydrate recognition events may have implications for effective nutrient uptake in the marine environment.

Publication types

  • Research Support, Non-U.S. Gov't

MeSH terms

  • Alteromonadaceae*
  • Amino Acid Sequence
  • Bacterial Proteins / chemistry*
  • Bacterial Proteins / metabolism*
  • Cell Wall / metabolism*
  • Ligands
  • Models, Molecular
  • Molecular Sequence Data
  • Phylogeny
  • Plant Cells*
  • Plants / metabolism
  • Protein Structure, Tertiary
  • Sequence Alignment
  • Terpenes / metabolism*

Substances

  • Bacterial Proteins
  • Ligands
  • Terpenes